Protein Data Bank File : 1f37a Title : ELECTRON TRANSPORT 31-MAY-00 1F37 Number of Amino Acid Residues : 109 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ALA GLU PHE LYS HIS VAL PHE VAL CYS VAL 10 GLN ASP ARG PRO PRO GLY HIS PRO GLN GLY 20 SER CYS ALA GLN ARG GLY SER ARG GLU VAL 30 PHE GLN ALA PHE MET GLU LYS ILE GLN THR 40 ASP PRO GLN LEU PHE MET THR THR VAL ILE 50 THR PRO THR GLY CYS MET ASN ALA CYS MET 60 MET GLY PRO VAL VAL VAL VAL TYR PRO ASP 70 GLY VAL TRP TYR GLY GLN VAL LYS PRO GLU 80 ASP VAL ASP GLU ILE VAL GLU LYS HIS LEU 90 LYS GLY GLY GLU PRO VAL GLU ARG LEU VAL 100 ILE SER LYS GLY LYS PRO PRO GLY MET Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ALA 0.0 -138.0 -176.8 2 GLU -151.8 -97.7 173.1 -51.7 152.2 0.1 3 PHE -167.6 128.0 -178.7 174.6 62.6 4 LYS -144.0 133.3 -179.7 -68.7 172.6 177.7 -69.9 5 HIS -113.1 113.4 -178.2 -162.0 160.2 6 VAL -98.3 126.1 180.0 -176.0 7 PHE -115.0 122.2 -179.8 -69.0 87.1 8 VAL -113.9 119.7 178.1 179.4 9 CYS -68.3 124.7 178.2 173.4 10 VAL -123.4 26.9 -179.8 -64.7 11 GLN -64.6 142.2 178.6 173.5 82.5 48.0 12 ASP -130.5 152.8 -179.5 -166.1 31.1 13 ARG -141.8 149.4 -179.8 -61.4 -163.8 178.3 93.6 14 PRO -54.8 154.9 -179.3 -23.2 36.2 15 PRO -50.5 -24.1 -176.5 -23.2 40.7 16 GLY -86.2 -17.9 -178.3 17 HIS -64.9 120.2 -179.5 -164.5 115.0 18 PRO -47.8 -43.7 -179.0 -27.9 41.3 19 GLN -73.6 -15.9 -178.7 -58.5 -166.0 162.0 20 GLY 61.1 -149.0 -179.5 21 SER -167.3 164.1 177.7 60.6 22 CYS -61.3 -36.2 179.8 -63.1 23 ALA -62.0 -34.0 178.9 24 GLN -75.4 -28.1 179.0 -83.9 165.4 -87.6 25 ARG -86.6 11.1 175.9 -59.3 -171.4 173.1 78.2 26 GLY 86.1 29.0 -178.0 27 SER -75.9 -22.2 178.0 68.3 28 ARG -69.8 -36.5 179.0 -58.8 -161.1 166.6 177.5 29 GLU -66.6 -37.5 178.1 -73.5 73.0 29.6 30 VAL -61.4 -49.1 179.2 168.7 31 PHE -57.0 -53.4 -178.0 175.9 71.8 32 GLN -60.1 -36.1 178.8 -62.0 163.5 -179.3 33 ALA -57.1 -55.0 -179.7 34 PHE -54.4 -41.7 -179.1 -84.3 98.9 35 MET -66.8 -25.2 179.9 -68.4 -51.8 -99.2 36 GLU -81.2 -23.8 -179.9 -60.7 -172.2 -56.8 37 LYS -78.4 -35.6 -179.6 -155.8 60.4 -173.8 176.3 38 ILE -68.3 -32.9 179.5 -65.4 -67.7 39 GLN -84.3 -33.1 -179.1 -77.8 -173.2 -68.5 40 THR -85.8 -1.7 179.4 -63.0 41 ASP -109.5 133.2 -179.9 -169.3 -66.6 42 PRO -55.9 -42.7 -176.8 -28.7 41.4 43 GLN -115.1 -14.5 -177.0 -45.2 157.0 -81.2 44 LEU -54.1 -45.5 179.1 -156.2 55.6 45 PHE -59.4 -19.5 -179.6 80.1 93.2 46 MET -71.2 -25.8 -179.6 -60.6 -164.5 -99.5 47 THR -136.6 28.4 -177.4 65.1 48 THR -148.8 136.7 178.2 -47.7 49 VAL -130.6 141.4 178.5 170.3 50 ILE -118.2 131.6 -179.9 -39.7 -62.4 51 THR -127.7 136.3 179.8 -47.5 52 PRO -87.1 137.5 -178.8 36.8 -40.7 53 THR -129.0 171.4 173.6 78.9 54 GLY -91.6 -177.3 -178.4 55 CYS -44.8 132.3 176.7 -161.6 56 MET -109.5 20.3 177.4 -65.1 -168.0 -89.2 57 ASN 61.2 40.6 178.0 -51.8 -67.2 58 ALA -143.8 37.1 -178.0 59 CYS -49.3 -36.9 -178.4 -45.6 60 MET -66.6 -25.0 179.3 75.2 152.9 63.7 61 MET -104.4 22.5 -179.2 -70.1 -53.9 -74.0 62 GLY -71.4 162.2 -0.5 63 PRO -63.7 133.7 -179.6 -32.2 46.0 64 VAL -99.1 135.7 -179.3 -176.7 65 VAL -137.0 122.3 179.6 175.0 66 VAL -113.9 140.8 178.7 46.9 67 VAL -120.3 120.0 178.0 178.0 68 TYR -111.9 162.7 0.1 -78.5 109.7 69 PRO -66.6 -13.3 -177.6 -18.7 34.4 70 ASP -46.2 -56.7 -177.6 -52.3 -176.4 71 GLY 93.6 30.2 -179.8 72 VAL -96.4 130.4 -178.9 177.9 73 TRP -109.8 126.8 179.9 -63.3 63.4 74 TYR -107.6 151.4 179.2 -75.4 107.6 75 GLY -133.8 152.6 179.4 76 GLN 52.5 43.7 178.5 -69.6 179.2 162.0 77 VAL -76.2 131.6 177.6 -179.0 78 LYS -108.8 157.7 179.7 -61.5 -179.9 169.8 -164.8 79 PRO -52.1 -45.0 -179.3 -30.9 42.7 80 GLU -64.9 7.0 179.3 51.9 -129.4 39.5 81 ASP -105.7 -25.1 -176.6 -71.2 -64.7 82 VAL -47.0 -51.9 -178.8 -176.6 83 ASP -51.1 -48.9 -179.5 -160.2 -70.2 84 GLU -65.7 -29.4 179.8 -170.3 -168.4 -21.0 85 ILE -73.5 -41.8 179.7 -69.0 -175.3 86 VAL -61.9 -55.6 -179.7 166.5 87 GLU -65.6 -61.8 -179.0 -65.3 -58.8 -62.8 88 LYS -61.5 -40.3 -177.8 -76.7 -77.7 -172.2 105.4 89 HIS -100.1 -63.1 -176.0 -172.4 -175.7 90 LEU -57.6 -27.1 178.6 -56.7 -169.0 91 LYS -107.8 -62.0 -179.6 -67.1 -174.5 -169.8 171.6 92 GLY -57.4 -25.1 -179.5 93 GLY 78.4 19.2 178.2 94 GLU -129.6 121.9 -179.8 65.8 -178.1 16.7 95 PRO -58.9 141.2 178.0 -32.5 43.6 96 VAL -82.7 79.7 -178.5 -179.0 97 GLU -38.1 -34.5 -179.7 -134.5 52.8 60.6 98 ARG -65.8 -11.1 -179.2 73.3 179.3 172.8 82.5 99 LEU -117.0 -7.8 -179.7 -65.9 -179.7 100 VAL -69.7 132.8 179.0 178.0 101 ILE -117.9 -11.1 177.4 58.0 -179.8 102 SER -171.2 163.5 179.0 -171.9 103 LYS -143.6 132.5 179.5 -75.5 -172.0 -178.1 -178.7 104 GLY 80.4 -28.7 179.0 105 LYS -148.5 159.2 -179.5 -67.6 -173.2 177.7 -178.5 106 PRO -60.8 152.6 180.0 -25.2 39.5 107 PRO -54.5 126.1 178.1 -28.1 41.1 108 GLY 81.1 26.2 178.9 109 MET -123.1 115.2 0.0 -173.4 172.8 -73.8 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ALA 64.236 29.501 6.948 2 GLU 60.843 28.311 5.556 3 PHE 58.899 25.214 6.852 4 LYS 60.153 21.679 6.987 5 HIS 58.646 18.487 8.409 6 VAL 61.268 15.877 9.319 7 PHE 60.188 12.247 9.748 8 VAL 62.461 9.798 11.510 9 CYS 61.607 6.066 11.464 10 VAL 61.958 4.751 15.033 11 GLN 60.424 1.361 14.325 12 ASP 61.799 -1.517 16.382 13 ARG 61.426 -5.289 16.014 14 PRO 62.367 -8.242 18.294 15 PRO 65.882 -9.722 17.932 16 GLY 64.698 -12.640 15.803 17 HIS 63.105 -10.666 12.967 18 PRO 65.315 -10.996 9.796 19 GLN 64.850 -7.370 8.629 20 GLY 65.879 -5.849 11.951 21 SER 64.827 -2.205 12.195 22 CYS 65.945 1.417 12.061 23 ALA 65.734 1.394 15.904 24 GLN 68.274 -1.441 15.981 25 ARG 70.377 0.563 13.561 26 GLY 70.337 3.454 15.980 27 SER 67.459 5.596 14.706 28 ARG 66.239 6.615 18.153 29 GLU 69.596 8.344 18.800 30 VAL 69.156 10.086 15.453 31 PHE 65.680 11.270 16.438 32 GLN 66.869 12.474 19.835 33 ALA 69.792 14.107 18.087 34 PHE 67.393 16.101 15.922 35 MET 65.327 16.969 18.977 36 GLU 68.431 18.244 20.755 37 LYS 69.083 20.352 17.695 38 ILE 65.571 21.820 17.738 39 GLN 65.970 23.020 21.335 40 THR 69.557 24.210 20.957 41 ASP 69.004 26.278 17.769 42 PRO 67.738 29.903 17.823 43 GLN 65.557 29.843 14.711 44 LEU 64.921 26.186 13.671 45 PHE 61.812 25.630 15.798 46 MET 60.287 28.536 13.899 47 THR 60.080 26.530 10.708 48 THR 60.647 22.926 11.793 49 VAL 58.884 19.911 13.277 50 ILE 60.355 16.457 13.844 51 THR 58.036 13.443 13.963 52 PRO 58.716 9.802 14.957 53 THR 57.238 7.114 12.685 54 GLY 56.785 3.412 12.269 55 CYS 58.333 1.647 9.240 56 MET 58.460 3.556 5.999 57 ASN 59.533 0.481 3.947 58 ALA 63.237 1.225 3.278 59 CYS 64.524 -0.914 6.126 60 MET 67.731 -2.025 4.372 61 MET 68.918 1.571 4.171 62 GLY 67.955 2.566 7.726 63 PRO 67.999 4.762 9.745 64 VAL 65.563 6.282 7.249 65 VAL 64.781 10.024 7.432 66 VAL 62.432 11.796 5.052 67 VAL 62.073 15.594 4.842 68 TYR 58.908 17.178 3.444 69 PRO 57.573 19.193 1.551 70 ASP 60.859 18.543 -0.204 71 GLY 60.347 14.796 -0.521 72 VAL 64.002 14.073 0.180 73 TRP 64.844 10.649 1.580 74 TYR 68.001 10.043 3.599 75 GLY 69.461 6.638 4.349 76 GLN 71.944 5.304 6.843 77 VAL 71.793 8.498 8.915 78 LYS 74.031 8.524 12.040 79 PRO 73.607 10.863 15.022 80 GLU 76.810 12.551 13.935 81 ASP 75.110 13.425 10.632 82 VAL 72.202 15.420 12.038 83 ASP 74.113 18.634 12.457 84 GLU 75.170 18.799 8.816 85 ILE 71.595 18.021 7.782 86 VAL 70.201 20.759 9.986 87 GLU 72.617 23.460 8.830 88 LYS 73.157 22.460 5.203 89 HIS 69.578 21.318 4.588 90 LEU 66.992 22.491 7.096 91 LYS 68.389 26.043 6.982 92 GLY 70.578 26.301 3.905 93 GLY 67.941 24.540 1.858 94 GLU 70.382 22.156 0.213 95 PRO 70.280 18.356 0.719 96 VAL 73.342 16.465 1.987 97 GLU 73.698 14.348 -1.174 98 ARG 76.013 11.699 0.305 99 LEU 73.054 10.426 2.374 100 VAL 70.223 10.956 -0.091 101 ILE 68.735 7.687 -1.342 102 SER 65.800 9.215 -3.143 103 LYS 63.834 12.337 -4.095 104 GLY 60.165 12.994 -4.682 105 LYS 59.281 9.307 -4.176 106 PRO 60.320 6.434 -1.869 107 PRO 63.501 4.451 -2.688 108 GLY 62.804 1.990 -5.504 109 MET 59.518 3.430 -6.713 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C S S S S S S S S S 10 S S S S S C C C C C 20 H H H H H H/H H H H H 30 H H H H H H H H H H 40 H/T T T T/T T T T/S S S S 50 S S S S S C C T T T 60 T C/P S S S S S/T T/P T T 70 S S S S S S/S S S S C 80 H H H H H H H H H/T T 90 T T S S S S/T T T T/S S 100 S S/T T T T S S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 E E E E E E e 10 t T T t T T t 20 t T T T T h H H H H 30 H H H H H H H H H H 40 h T g G G G e E E E 50 E E E S S g G G 60 G g S e E E E E T T 70 e E E E e S g G G 80 h H H H H H H H h T 90 T T t g G G e E 100 E E E e S t T T t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ALA 59.9 82.4 71.5 2 GLU 41.5 29.9 73.2 3 PHE 70.8 42.4 64.3 4 LYS 165.3 95.3 58.3 5 HIS 100.5 66.9 49.2 6 VAL 118.8 100.0 27.0 7 PHE 120.5 72.2 48.5 8 VAL 118.8 100.0 36.5 9 CYS 97.7 98.5 49.5 10 VAL 89.5 75.4 55.7 11 GLN 91.8 61.8 62.6 12 ASP 59.1 53.5 68.4 13 ARG 173.7 83.2 49.1 14 PRO 28.4 22.8 71.4 15 PRO 17.3 13.9 83.9 16 GLY 0.0 0.0 83.0 17 HIS 82.5 54.9 63.0 18 PRO 21.7 17.5 81.7 19 GLN 56.5 38.0 74.6 20 GLY 26.2 75.4 75.4 21 SER 83.0 99.3 65.4 22 CYS 96.1 96.9 44.6 23 ALA 70.5 97.1 68.5 24 GLN 81.8 55.1 76.5 25 ARG 122.5 58.7 73.2 26 GLY 15.8 45.3 83.0 27 SER 83.6 100.0 44.0 28 ARG 87.1 41.7 75.2 29 GLU 52.3 37.7 68.3 30 VAL 118.6 99.9 32.5 31 PHE 130.3 78.1 39.4 32 GLN 49.5 33.3 66.7 33 ALA 58.4 80.5 58.3 34 PHE 166.2 99.7 23.6 35 MET 81.5 51.1 60.3 36 GLU 23.4 16.9 80.0 37 LYS 126.0 72.7 59.8 38 ILE 119.9 83.5 44.2 39 GLN 10.7 7.2 88.6 40 THR 15.1 14.1 84.4 41 ASP 103.0 93.2 55.2 42 PRO 26.9 21.6 84.6 43 GLN 43.3 29.1 70.0 44 LEU 146.8 99.3 43.4 45 PHE 59.2 35.5 74.4 46 MET 72.4 45.4 65.5 47 THR 83.9 78.5 64.8 48 THR 106.9 100.0 41.1 49 VAL 45.3 38.1 68.8 50 ILE 142.5 99.3 30.8 51 THR 67.1 62.7 54.1 52 PRO 70.7 56.8 53.7 53 THR 81.4 76.1 52.5 54 GLY 9.9 28.6 76.2 55 CYS 79.4 80.1 59.9 56 MET 129.0 81.0 52.3 57 ASN 11.5 9.5 79.3 58 ALA 62.1 85.6 46.0 59 CYS 84.1 84.8 64.2 60 MET 10.6 6.6 81.7 61 MET 102.4 64.3 57.2 62 GLY 34.8 100.0 49.7 63 PRO 116.1 93.3 46.7 64 VAL 117.0 98.5 38.7 65 VAL 118.8 100.0 29.6 66 VAL 116.5 98.1 34.1 67 VAL 118.8 100.0 40.7 68 TYR 91.0 50.3 56.8 69 PRO 46.4 37.3 70.4 70 ASP 72.5 65.6 62.3 71 GLY 31.9 91.6 54.4 72 VAL 111.3 93.7 38.6 73 TRP 191.4 93.4 42.0 74 TYR 181.0 100.0 33.5 75 GLY 34.8 100.0 51.5 76 GLN 53.9 36.3 71.5 77 VAL 118.8 100.0 35.8 78 LYS 52.9 30.5 75.3 79 PRO 73.3 58.9 57.4 80 GLU 28.1 20.3 76.1 81 ASP 104.3 94.4 55.1 82 VAL 114.6 96.5 36.7 83 ASP 41.4 37.5 70.3 84 GLU 78.0 56.3 67.8 85 ILE 143.3 99.9 28.8 86 VAL 118.5 99.7 32.5 87 GLU 72.7 52.5 71.3 88 LYS 66.4 38.3 75.6 89 HIS 149.5 99.5 45.3 90 LEU 147.7 99.9 27.7 91 LYS 118.6 68.4 72.5 92 GLY 5.3 15.2 78.5 93 GLY 25.9 74.5 76.6 94 GLU 48.2 34.8 68.0 95 PRO 98.5 79.1 57.3 96 VAL 108.5 91.3 52.1 97 GLU 47.5 34.2 72.5 98 ARG 82.2 39.3 75.6 99 LEU 131.9 89.2 57.8 100 VAL 111.2 93.6 53.1 101 ILE 119.1 83.0 44.0 102 SER 61.2 73.2 58.0 103 LYS 80.1 46.2 69.7 104 GLY 5.1 14.6 75.2 105 LYS 40.5 23.4 74.6 106 PRO 85.5 68.7 41.1 107 PRO 102.8 82.6 45.1 108 GLY 0.0 0.0 85.2 109 MET 49.0 30.7 69.6